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Chemical genetics of AGC-kinases reveals shared targets of Ypk1, Protein Kinase A and Sch9

View ORCID ProfileMichael Plank, Mariya Perepelkina, Markus Müller, Stefania Vaga, Xiaoming Zou, Marina Berti, Jacques Saarbach, Steven Haesendonckx, Nicolas Winssinger, Ruedi Aebersold, Robbie Loewith
doi: https://doi.org/10.1101/756841
Michael Plank
1Department of Molecular Biology, University of Geneva, CH-1211, Geneva, Switzerland
4National Centre of Competence in Research - Chemical Biology, University of Geneva, CH-1211, Geneva, Switzerland
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  • ORCID record for Michael Plank
  • For correspondence: michael.plank@unige.ch
Mariya Perepelkina
1Department of Molecular Biology, University of Geneva, CH-1211, Geneva, Switzerland
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Markus Müller
4National Centre of Competence in Research - Chemical Biology, University of Geneva, CH-1211, Geneva, Switzerland
6Swiss Institute of Bioinformatics, CH-1015 Lausanne, Switzerland
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Stefania Vaga
2Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, CH-8093 Zürich, Switzerland
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Xiaoming Zou
1Department of Molecular Biology, University of Geneva, CH-1211, Geneva, Switzerland
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Marina Berti
1Department of Molecular Biology, University of Geneva, CH-1211, Geneva, Switzerland
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Jacques Saarbach
4National Centre of Competence in Research - Chemical Biology, University of Geneva, CH-1211, Geneva, Switzerland
5Department of Organic Chemistry, University of Geneva, CH-1211, Geneva, Switzerland
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Steven Haesendonckx
1Department of Molecular Biology, University of Geneva, CH-1211, Geneva, Switzerland
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Nicolas Winssinger
4National Centre of Competence in Research - Chemical Biology, University of Geneva, CH-1211, Geneva, Switzerland
5Department of Organic Chemistry, University of Geneva, CH-1211, Geneva, Switzerland
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Ruedi Aebersold
2Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, CH-8093 Zürich, Switzerland
3Faculty of Science, University of Zurich, CH-8006, Zurich, Switzerland
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Robbie Loewith
1Department of Molecular Biology, University of Geneva, CH-1211, Geneva, Switzerland
4National Centre of Competence in Research - Chemical Biology, University of Geneva, CH-1211, Geneva, Switzerland
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ABSTRACT

Protein phosphorylation cascades play a central role in the regulation of cell growth and protein kinases PKA, Sch9 and Ypk1 take centre stage in regulating this process in S. cerevisiae. To understand how these kinases co-ordinately regulate cellular functions we compared the phospho-proteome of exponentially growing cells without and with acute chemical inhibition of PKA, Sch9 and Ypk1. Sites hypo-phosphorylated upon PKA and Sch9 inhibition were preferentially located in RRxS/T-motifs suggesting that many are directly phosphorylated by these enzymes. Interestingly, when inhibiting Ypk1 we not only detected several hypo-phosphorylated sites in the previously reported RxRxxS/T-, but also in an RRxS/T-motif. Validation experiments revealed that neutral trehalase Nth1, a known PKA target, is additionally phosphorylated and activated downstream of Ypk1. Signalling through Ypk1 is therefore more closely related to PKA- and Sch9-signalling than previously appreciated and may perform functions previously only attributed to the latter kinases.

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Posted September 04, 2019.
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Chemical genetics of AGC-kinases reveals shared targets of Ypk1, Protein Kinase A and Sch9
Michael Plank, Mariya Perepelkina, Markus Müller, Stefania Vaga, Xiaoming Zou, Marina Berti, Jacques Saarbach, Steven Haesendonckx, Nicolas Winssinger, Ruedi Aebersold, Robbie Loewith
bioRxiv 756841; doi: https://doi.org/10.1101/756841
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Chemical genetics of AGC-kinases reveals shared targets of Ypk1, Protein Kinase A and Sch9
Michael Plank, Mariya Perepelkina, Markus Müller, Stefania Vaga, Xiaoming Zou, Marina Berti, Jacques Saarbach, Steven Haesendonckx, Nicolas Winssinger, Ruedi Aebersold, Robbie Loewith
bioRxiv 756841; doi: https://doi.org/10.1101/756841

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